ID A0A0F7IG59_9EURY Unreviewed; 466 AA.
AC A0A0F7IG59;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE SubName: Full=Pyruvate 2-oxoglutarate dehydrogenase complex {ECO:0000313|EMBL:AKG91574.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:AKG91574.1};
GN ORFNames=GAH_01110 {ECO:0000313|EMBL:AKG91574.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91574.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG91574.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG91574.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CP011267; AKG91574.1; -; Genomic_DNA.
DR RefSeq; WP_048095197.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7IG59; -.
DR STRING; 113653.GAH_01110; -.
DR GeneID; 24803684; -.
DR KEGG; gah:GAH_01110; -.
DR PATRIC; fig|113653.22.peg.1103; -.
DR HOGENOM; CLU_016755_1_2_2; -.
DR InParanoid; A0A0F7IG59; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000034723; Chromosome.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691}; Pyruvate {ECO:0000313|EMBL:AKG91574.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000034723}.
FT DOMAIN 4..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..448
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 466 AA; 51718 MW; 5125894768B044B4 CRC64;
MNEYDAIVIG TGSAMIIAGR ILSENPEARV AVVDKDDAGG ICLTRGCIPS KLVISPAEIL
YDLEKMRDFI DAKVRGVNFG RVMRRMREKV DRESRMIEES LRRSENINYF KDVAEFVDRY
TLKVRGKEIK SDRIFIGSGS RPLVPGIKGL REAGYLTSDT ILRLEEMPES MVIIGGGYIA
VEYGNFFARA GCDVRIVEMM PRILSNEEPE VSEVVQRELE RHAEIYTSHR VVEVRRDGEV
RRVVAQGESG KVEVEGEVVL VAVGREPNSD VLRPERGGVE TDERGWIKVN SHLETSVKGV
YAIGDANGKH MFRHVANREA VIAYENAFRN AGIEMDYSAM PHAIFTQPEV GSVGLREDEA
VERFGKGNVL IGYEELRSTG KGLAMNADGF AKVIVHRDGR ILGAHIVGKS ASILVQEVAT
LMAIGASYHA ALHALHIHPA LSEVVSWAFG NLMSVEEYRK FISRNT
//
